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Nucleic Acids Research, 1981, Vol. 9, No. 14 3465-3481
© 1981

MOLECULAR BIOLOGY

The proteins of the messenger RNA binding site of Escherichia coli ribosomes

O.I. Gimautdinova, G.G. Karpova, D.G. Knorre and N.D. Kobetz

Institute of Organic Chemistry, Siberian Division of the Academy of Sciences of the USSR Novosibirsk, 630090, USSR

Received June 8, 1981. Oligo(U) derivatives with [14C]-4-(N-2-chloroethyl-Nmethylamino) benzaldehyde attached to 3'-end cis-diol group via acetal bond, p(Up)n-1 UCHRC1 as well as with [14C]-4-(N-2-chloroethyl-N-methylamino)benzylamine attached to 5'-phosphate via amide bond, ClRCH2MpU(pU)6 were used to modify 70S E.coli ribosomes near mRNA binding centre. Within ternary complex with ribosome and tRNAPhe all reagents covalently bind to ribosome the extent of modification being 0.1–0.4 mole/mole 70S. p(Up)n–1UCHRCl alkylates either 30S (n=5,7) or both subunits (n=5,8). rRNA is preferentially modified within 30S 3ubunit. ClRCH2MHpU (pU)6 alkylates both subunits the proteins being mainly modified. The distribution of the label among proteins differ for various reagents. S4, S5, S7, S9, S11, S13, S15, S18 and S21 are found to be alkylated within 30S subunit, proteins L1, L2, L6, L7/L12, L19, L31 and L32 are modified in the 50S subunit.

Most proteins modified within 30S subunit are located at the "head" of this subunit and proteins modified within 50S subunit are located at the surface of the contact between this subunit and the "head" of 30S subunit at the model of Stoffler.


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